Selective binding of zinc ions to heparin rather than to other glycosaminoglycans.
The relative binding affinity of Zn2+ to several glycosaminoglycans was determined by gel-filtration chromatography. Binding was observed only between Zn2+ and heparin. No binding was observed between Zn2+ and chondroitin 4-sulphate, chondroitin 6-sulphate, dermatan sulphate of hyaluronic acid. All of the glycosaminoglycans contained carboxy groups, but only heparin bound Zn2+. This observation suggests that, contrary to a previously proposed hypothesis, simple electrostatic interactions between the negatively charged carboxy groups of the glycosaminoglycans and the positively charged Zn2+ cannot explain the observed binding.
D002809:Chondroitin Sulfates / Q000378:metabolism; D002850:Chromatography, Gel; D003871:Dermatan Sulfate / Q000378:metabolism; D006025:Glycosaminoglycans / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D006820:Hyaluronic Acid / Q000378:metabolism; D015032:Zinc / Q000378:metabolism*
D006025:Glycosaminoglycans; D003871:Dermatan Sulfate; D006820:Hyaluronic Acid; D006493:Heparin; D002809:Chondroitin Sulfates; D015032:Zinc